The DOI matches its Crossref record; 44 of the 45 references it cites were found in a registry or an index.
Mediators of endoplasmic reticulum stress-induced apoptosis
Open accessAbstract
The efficient functioning of the endoplasmic reticulum (ER) is essential for most cellular activities and survival. Conditions that interfere with ER function lead to the accumulation and aggregation of unfolded proteins. ER transmembrane receptors detect the onset of ER stress and initiate the unfolded protein response (UPR) to restore normal ER function. If the stress is prolonged, or the adaptive response fails, apoptotic cell death ensues. Many studies have focused on how this failure initiates apoptosis, as ER stress-induced apoptosis is implicated in the pathophysiology of several neurodegenerative and cardiovascular diseases. In this review, we examine the role of the molecules that are activated during the UPR in order to identify the molecular switch from the adaptive phase to apoptosis. We discuss how the activation of these molecules leads to the commitment of death and the mechanisms that are responsible for the final demise of the cell.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Alterations of ER redox state may also influence the cell death machinery by inducing caspase-dependent apoptosis through the down-regulation of Bcl-2 protein, which physiologically blocks the apoptotic cell death [52]”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
Proapoptotic BAX and BAK Modulate the Unfolded Protein Response by a Direct Interaction with IRE1α
Hetz, C. A., Bernasconi, P., Fisher, J. K., Lee, A., Bassik, M. C., Antonsson, B. E., Brandt, G. S., Iwakoshi, N. N., Schinzel, A. C., Glimcher, L. H., et al. (2006) · Science · doi:10.1126/science.1123480 · Cited by 688
RetractedControl of inositol 1,4,5-trisphosphate-induced Ca2+ release by cytosolic Ca2+
Bootman, M. D., Missiaen, L., Parys, J. B., SMEDT, H. D., & Casteels, R. (1995) · Biochemical Journal · doi:10.1042/bj3060445 · Cited by 5,131
Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
Proapoptotic BAX and BAK: A Requisite Gateway to Mitochondrial Dysfunction and Death
Wei, M. C., Zong, W.-X., Cheng, E. H.-Y., Lindsten, T., Panoutsakopoulou, V., Ross, A. J., Roth, K. A., MacGregor, G. R., Thompson, C. B., & Korsmeyer, S. J. (2001) · Science · doi:10.1126/science.1059108 · Cited by 3,988
Mutation of the mouse klotho gene leads to a syndrome resembling ageing
Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,292
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,099
Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y.-H., Chung, P., Harding, H., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 3,081
Cited by
Sorted by citations
Items 701–800 of 1,004
Liu, L., Fan, Z., Tang, Y., & Ke, Z. (2013) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.12311 · Cited by 47
Lu, X., Li, Y., Wang, W., Chen, S., Liu, T., Jia, D., Quan, X., Sun, D., Chang, A. K., & Gao, B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086753 · Cited by 47
Min, K., Jung, K.-J., & Kwon, T. K. (2014) · Journal of Cancer Prevention · doi:10.15430/jcp.2014.19.3.170 · Cited by 47
Yang, Y., Lin, X., Huang, H., Feng, D., Ba, Y., Cheng, X., & Cui, L. (2015) · Journal of Environmental Sciences · doi:10.1016/j.jes.2014.11.004 · Cited by 47
Li, G., Petiwala, S. M., Nonn, L., & Johnson, J. J. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.09.054 · Cited by 47
Ding, Y., Zou, J., Li, Z., Tian, J., Abdelalim, S., Du, F., She, R., Wang, D., Tan, C., Wang, H., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020008 · Cited by 47
Diet-Induced Unresolved ER Stress Hinders KRAS-Driven Lung Tumorigenesis
Ramadori, G., Konstantinidou, G., Venkateswaran, N., Biscotti, T., Morlock, L., Galiè, M., Williams, N. S., Luchetti, M. M., Santinelli, A., Scaglioni, P. P., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.11.020 · Cited by 50
Belkaid, A., Fortier, S., Cao, J. P., & Annabi, B. (2007) · Neoplasia · doi:10.1593/neo.07142 · Cited by 50
Endoplasmic Reticulum Stress in Arterial Smooth Muscle Cells: A Novel Regulator of Vascular Disease
Shanahan, C. M., & Furmanik, M. (2016) · Current Cardiology Reviews · doi:10.2174/1573403x12666161014094738 · Cited by 48
Cai, J., Lin, Y., Zhang, H., Liang, J., Tan, Y., Cavenee, W. K., & Yan, G. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1701002114 · Cited by 50
Bavachin Induces Apoptosis through Mitochondrial Regulated ER Stress Pathway in HepG2 Cells
Yang, Y. C., Tang, X., Hao, F., Ma, Z.-C., Wang, Y., Wang, L., & Gao, Y. (2017) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b17-00672 · Cited by 48
Hentilä, J., Ahtiainen, J. P., Paulsen, G., Raastad, T., Häkkinen, K., Mero, A. A., & Hulmi, J. J. (2018) · Acta Physiologica · doi:10.1111/apha.13069 · Cited by 50
Yang, Y., Dong, F., Liu, X., Xu, J., Wu, X., Liu, W., & Zheng, Y. (2018) · Environmental Pollution · doi:10.1016/j.envpol.2018.09.041 · Cited by 47
Pagáčová, E., Štefančíková, L., Schmidt-Kaler, F. D. F., Hildenbrand, G. L., Vičar, T., Depeš, D., Lee, J., Bestvater, F., Lacombe, S., Porcel, E., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030588 · Cited by 47
Tan, L. P., Register, T. C., & Yammani, R. R. (2020) · Aging and Disease · doi:10.14336/ad.2019.1130 · Cited by 48
Srinivasan, K. K., & Sharma, S. S. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.07.004 · Cited by 47
Xia, B., Li, Q., Zheng, K., Wu, J., Huang, C., Liu, K., You, Q., & Yuan, X. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175864 · Cited by 47
Ozasa, R., Okada, T., Nadanaka, S., Nagamine, T., Zyryanova, A., Harding, H. P., Ron, D., & Mori, K. (2013) · Cell Structure and Function · doi:10.1247/csf.13012 · Cited by 46
Xu, L., Liu, J., Zhang, J., Zhang, N., & Wang, Z. (2014) · Cancer Research and Treatment · doi:10.4143/crt.2013.222 · Cited by 46
Zhang, Q., Yu, J., Liu, B., Lv, Z., Xia, T., Xiao, F., Chen, S., & Guo, F. (2013) · Diabetes · doi:10.2337/db12-1050 · Cited by 47
Targeting GRP78 to enhance melanoma cell death
Martin, S., Hill, D. S., Paton, J. C., Paton, A. W., Birch‐Machin, M. A., Lovat, P. E., & Redfern, C. P. F. (2010) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2010.00731.x · Cited by 46
Chevronnay, H. P. G., Janssens, V., Smissen, P. V. D., Liao, X. H., Abid, Y., Névo, N., Antignac, C., Refetoff, S., Cherqui, S., Pierreux, C. E., et al. (2015) · Endocrinology · doi:10.1210/en.2014-1672 · Cited by 46
Lei, P., Abdelrahim, M., Cho, S. D., Liu, S., Chintharlapalli, S. R., & Safe, S. H. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn103 · Cited by 46
Shah, A. B., Vaidya, N. K., Bhat, H. K., & Kumar, A. (2016) · Scientific Reports · doi:10.1038/srep18929 · Cited by 48
Jiang, M., Yun, Q., Shi, F., Niu, G., Gao, Y., Xie, S., & Yu, S. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00226.2015 · Cited by 46
Wang, S., Lee, A. C.-L., Chen, I., Chang, N., Wu, H., Yu, H., Chang, Y., Lee, T., Yu, J., Yu, A. L.-T., et al. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.03.050 · Cited by 46
Mohammed‐Ali, Z., Lü, C., Marway, M. K., Carlisle, R. E., Ask, K., Lukic, D., Krepinsky, J. C., & Dickhout, J. G. (2017) · Scientific Reports · doi:10.1038/srep41572 · Cited by 46
Up-Regulated ATF4 Expression Increases Cell Sensitivity to Apoptosis in Response to Radiation
Zong, Y., Feng, S., Cheng, J.-W., Yu, C., & GuoCai, L. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000458742 · Cited by 46
Zhang, C., Tang, Y., Li, Y., Xie, L., Zhuang, W., Liu, J., & Gong, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179042 · Cited by 45
Lipid-induced endoplasmic reticulum stress in X-linked adrenoleukodystrophy
van de Beek, M.-C., Ofman, R., Dijkstra, I. M. E., Wijburg, F. A., Engelen, M., Wanders, R. J. A., & Kemp, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.06.003 · Cited by 48
Calcium Signaling Deficits in Glia and Autophagic Pathways Contributing to Neurodegenerative Disease
Mustaly-Kalimi, S., Littlefield, A. M., & Stutzmann, G. E. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7266 · Cited by 47
Quantitative assessment of cell fate decision between autophagy and apoptosis
Liu, B., Oltvai, Z. N., Bayır, H., Silverman, G. A., Pak, S. C., Perlmutter, D. H., & Bahar, İ. (2017) · Scientific Reports · doi:10.1038/s41598-017-18001-w · Cited by 47
Mechanisms contributing to adverse outcomes of COVID-19 in obesity
Sudhakar, M., Beaula, W. S., Meiyazhagan, G., & Parvathi, V. D. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04356-w · Cited by 50
Dunham, R. A. (2008) · Comparative Immunology Microbiology and Infectious Diseases · doi:10.1016/j.cimid.2007.11.006 · Cited by 46
Mitochondria, endoplasmic reticulum, and alternative pathways of cell death in critical illness
Yasuhara, S., Asai, A., Sahani, N., & Martyn, J. A. J. (2007) · Critical Care Medicine · doi:10.1097/01.ccm.0000278045.91575.30 · Cited by 47
Kwong, W., Sun, R. W., Lok, C., Siu, F., Wong, S.-Y., Low, K., & Che, C. (2012) · Chemical Science · doi:10.1039/c2sc21541a · Cited by 46
How Bacteria-Induced Apoptosis of Intestinal Epithelial Cells Contributes to Mucosal Inflammation
Hausmann, M. (2010) · International Journal of Inflammation · doi:10.4061/2010/574568 · Cited by 48
Molecular Mechanisms of Pesticide Toxicity
Tebourbi, O., Sakly, M., & Rhouma, K. B. (2011) · InTech eBooks · doi:10.5772/17952 · Cited by 46
Redox‐based endoplasmic reticulum dysfunction in neurological diseases
Bánhegyi, G., Mandl, J., & Csala, M. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05571.x · Cited by 45
Mechanisms and Consequences of Injury and Repair in Older Organ Transplants
Slegtenhorst, B. R., Dor, F. J. M. F., Elkhal, A., Biefer, H. R. C., Yang, X., Edtinger, K., Quante, M., Chong, A. S., & Tullius, S. G. (2014) · Transplantation · doi:10.1097/tp.0000000000000072 · Cited by 45
Storniolo, A., Raciti, M., Cucina, A., Bizzarri, M., & Renzo, L. D. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/645157 · Cited by 45
Sarkey, J. P., Chu, M.-S., McShane, M., Bovo, E., Mou, Y. A., Zima, A., de Tombe, P., Kartje, G. L., & Martin, J. L. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.03.004 · Cited by 45
Minicis, S. D., Candelaresi, C., Agostinelli, L., Taffetani, S., Saccomanno, S., Rychlicki, C., Trozzi, L., Marzioni, M., Benedetti, A., & Svegliati‐Baroni, G. (2012) · Liver International · doi:10.1111/j.1478-3231.2012.02860.x · Cited by 47
Yu, S. J., Yoon, J., Yang, J. I., Cho, E. J., Kwak, M. S., Jang, E. S., Lee, J., Kim, Y. J., Lee, H.-S., & Kim, C. Y. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9416-5 · Cited by 45
Shah, A. B., & Kumar, A. (2016) · Oncotarget · doi:10.18632/oncotarget.10025 · Cited by 45
Reciprocal regulation between ER stress and autophagy in renal tubular fibrosis and apoptosis
Shu, S., Wang, H., Zhu, J., Liu, Z., Yang, D., Wu, W., Cai, J., Chen, A., Tang, C., & Dong, Z. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04274-7 · Cited by 48
Gharibani, P. M., Modi, J., Menzie, J., Alexandrescu, A., Ma, Z., Tao, R., Prentice, H. M., & Wu, J. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.05.042 · Cited by 46
Su, Y.-C., Wu, J., & Hong, J. (2010) · APOPTOSIS · doi:10.1007/s10495-010-0565-x · Cited by 45
LaRosa, P. C., Riethoven, J.-J. M., Chen, H., Xia, Y., Zhou, Y., Chen, M., Miner, J. L., & Fromm, M. (2007) · Physiological Genomics · doi:10.1152/physiolgenomics.00156.2007 · Cited by 46
Zhong, Y., Jin, C., Han, J., Zhu, J., Liu, Q., Sun, D., Xia, X., & Peng, X. (2021) · Cell Biology and Toxicology · doi:10.1007/s10565-021-09589-x · Cited by 44
Huang, R., Li, G., Wang, K., Wang, Z., Zeng, F., Hu, H., & Jiang, T. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.619396 · Cited by 44
Cardiovascular Consequences of Uremic Metabolites: an Overview of the Involved Signaling Pathways
Curaj, A., Vanholder, R. C., Loscalzo, J., Quach, K., Wu, Z., Jankowski, V., & Jankowski, J. (2024) · Circulation Research · doi:10.1161/circresaha.123.324001 · Cited by 48
Zhong, S., Sun, Z., Tian, Q., Wen, W., Chen, F., Huang, X., & Li, Y. (2024) · The FASEB Journal · doi:10.1096/fj.202400969rr · Cited by 44
Shimada, Y., Kobayashi, H., Kawagoe, S., Aoki, K., Kaneshiro, E., Shimizu, H., Eto, Y., Ida, H., & Ohashi, T. (2011) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2011.09.005 · Cited by 44
Involvement of endoplasmic reticulum stress in homocysteine-induced apoptosis of osteoblastic cells
Park, S.-J., Kim, K., Kim, W., Oh, I., & Cho, C. (2012) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-011-0346-9 · Cited by 44
Li, L., Wang, L., Xiao, R., Zhu, G., Li, Y., Liu, C., Yang, R., Tang, Z., Li, J., Huang, W., et al. (2011) · Bioscience Reports · doi:10.1042/bsr20110069 · Cited by 44
Zhang, R., Wang, R., Chen, Q., & Chang, H. (2015) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3588 · Cited by 44
Sari, F. R., Watanabe, K., Thandavarayan, R. A., Harima, M., Zhang, S., Muslin, A. J., Kodama, M., & Aizawa, Y. (2010) · Journal of Pharmacological Sciences · doi:10.1254/jphs.10047fp · Cited by 43
Differential cell death regulation between adult-unloaded and aged rat soleus muscle
Ogata, T., Machida, S., Oishi, Y., Higuchi, M., & Muraoka, I. (2009) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2009.02.001 · Cited by 44
Kim, B. M., Maeng, K., Lee, K.-H., & Hong, S. H. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.09.014 · Cited by 44
van Vliet, A. R., Martin, S., Garg, A. D., & Agostinis, P. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.03.010 · Cited by 44
Deregulation of Pancreas-Specific Oxidoreductin ERO1β in the Pathogenesis of Diabetes Mellitus
Awazawa, M., Futami, T., Sakada, M., Kaneko, K., Ohsugi, M., Nakaya, K., Terai, A., Suzuki, R., Koike, M., Uchiyama, Y., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01647-13 · Cited by 43
Li, K., Zhang, H., Qiu, J., Lin, Y., Liang, J., Xiao, X., Fu, L., Wang, F., Cai, J., Tan, Y., et al. (2015) · Molecular Therapy · doi:10.1038/mt.2015.172 · Cited by 44
ER stress disturbs SR/ER-mitochondria Ca2+ transfer: Implications in Duchenne muscular dystrophy
Pauly, M., Angebault, C., Dridi, H., Notarnicola, C., Scheuermann, V., Lacampagne, A., Matecki, S., & Fauconnier, J. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.06.009 · Cited by 46
Li, Y., Chen, Y., Huang, H., Shi, M., Yang, W., Kuang, J., & Yan, J. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3145 · Cited by 44
Piperine ameliorates SCA17 neuropathology by reducing ER stress
Guo, J., Cui, Y., Liu, Q., Yang, Y., Li, Y., Weng, L., Tang, B., Jin, P., Li, X., Yang, S., et al. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0236-x · Cited by 44
Melatonin receptor depletion suppressed hCG-induced testosterone expression in mouse Leydig cells
Gao, Y., Wu, X., Zhao, S., Zhang, Y., Ma, H., Yang, Z., Yang, W., Zhao, C., Wang, L., & Zhang, Q. (2019) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-019-0147-z · Cited by 44
Xue, X., Quan, Y., Gong, L., Gong, X., & Li, Y. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.113121 · Cited by 44
The regulatory role of insulin in energy metabolism and leukocyte functions
Cruz-Pineda, W. D., Parra‐Rojas, I., Rodríguez-Ruiz, H. A., Illades‐Aguiar, B., Matia‐García, I., & Garibay‐Cerdenares, O. L. (2021) · Journal of Leukocyte Biology · doi:10.1002/jlb.2ru1220-847r · Cited by 49
Jang, H., Jun, Y., Kim, S., Kim, E., Jung, Y., Park, B. J., Lee, J., Kim, J., Lee, S., & Kim, J. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03675-y · Cited by 42
Wang, W., Sun, Y., Chen, S., Zhou, X., Wu, X., Kong, W., & Kong, W. (2015) · Experimental Gerontology · doi:10.1016/j.exger.2015.07.003 · Cited by 45
Lee, W., & Thévenod, F. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.07.004 · Cited by 44
Wu, C., Sheu, M., Tsai, K., Weng, T., Chiang, C., & Liu, S. (2010) · Toxicological Sciences · doi:10.1093/toxsci/kfq006 · Cited by 44
Zhang, Y., Liu, M., Peng, B., Jia, S., Koh, D., Wang, Y., Cheng, H. S., Tan, N. S., Warth, B., Chen, D., et al. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.0c02188 · Cited by 42
Arthropods Under Pressure: Stress Responses and Immunity at the Pathogen-Vector Interface
Rosche, K. L., Sidak‐Loftis, L. C., Hurtado, J., Fisk, E. A., & Shaw, D. K. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.629777 · Cited by 40
Mafi, S., Ahmadi, E., Meehan, E. V., Chiari, C. C., Mansoori, B., Sadeghi, H., Milani, S., Jafarinia, M., Taeb, S., Bashmagh, B. M., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-3032 · Cited by 43
Endoplasmic Reticulum Stress and Its Impact on Adipogenesis: Molecular Mechanisms Implicated
Kim, G., Lee, J., Ha, J., Kang, I., & Choe, W. (2023) · Nutrients · doi:10.3390/nu15245082 · Cited by 47
Gong, W., Duan, Q., Cai, Z., Chen, C., Ni, L., Yan, M., Wang, X., Cianflone, K., & Wang, D. W. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12346 · Cited by 43
Shin, H.-S., Ryu, E., Oh, E., & Kang, D. (2015) · Laboratory Investigation · doi:10.1038/labinvest.2015.91 · Cited by 43
Review: retinal degeneration: focus on the unfolded protein response.
Gorbatyuk, M. S., & Gorbatyuk, O. S. (2013) · Europe PMC (PubMed Central) · Cited by 43
Guo, F., Liu, Y., Zhou, J., Luo, S., Zhao, W., Li, X., & Liu, C.-J. (2012) · Histochemistry and Cell Biology · doi:10.1007/s00418-012-0967-7 · Cited by 43
RetractedDifferential Effects of Procaspase-3 Activating Compounds in the Induction of Cancer Cell Death
West-Szymanski, D. C., Qin, Y., Peterson, Q. P., Thomas, D., Palchaudhuri, R., Morrison, K. C., Lucas, P. W., Palmer, A. E., Fan, T. M., & Hergenrother, P. J. (2012) · Molecular Pharmaceutics · doi:10.1021/mp200673n · Cited by 43
Krajarng, A., Imoto, M., Tashiro, E., Fujimaki, T., Shinjo, S., & Watanapokasin, R. Y. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0544-4 · Cited by 43
Seong, Y.-A., Shin, P.-G., Yoon, J., Yadunandam, A. K., & Kim, G. (2013) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-013-9717-2 · Cited by 43
Zhong, W., Chen, X., Jiang, P., Wan, J. M. F., Qin, P., & Yu, A. C. H. (2013) · Ultrasound in Medicine & Biology · doi:10.1016/j.ultrasmedbio.2013.08.005 · Cited by 45
Kim‐Han, J. S., & O’Malley, K. L. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1791 · Cited by 43
Ca2+, autophagy and protein degradation: Thrown off balance in neurodegenerative disease
Vicencio, J. M., Lavandero, S., & Szabadkai, G. (2010) · Cell Calcium · doi:10.1016/j.ceca.2009.12.013 · Cited by 44
Su, T.-R., Tsai, F., Lin, J., Huang, H. H., Chiu, C., Su, J., Yang, Y., Chen, J. Y., Wong, B.-S., & Wu, Y. (2012) · Marine Drugs · doi:10.3390/md10081883 · Cited by 43
Liu, X., Wang, M., Chen, H., Guo, Y., Ma, F., Shi, F., Bi, Y., & Li, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053431 · Cited by 43
RetractedTransforming growth factor-β1 causes pulmonary microvascular endothelial cell apoptosis via ALK5
Lü, Q., Patel, B., Harrington, E. O., & Rounds, S. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.90307.2008 · Cited by 43
ELANE mutant–specific activation of different UPR pathways in congenital neutropenia
Nustede, R., Klimiankou, M., Klimenkova, O., Kuznetsova, I., Zeidler, C., Welte, K., & Skokowa, J. (2015) · British Journal of Haematology · doi:10.1111/bjh.13823 · Cited by 43
Kong, S., Yang, Y., Xu, Y., Wang, Y., Zhang, Y., Melo‐Cardenas, J., Xu, X., Gao, B., Thorp, E. B., Zhang, D. D., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606742113 · Cited by 43
Arumughan, A., Roske, Y., Barth, C., Lleras-Forero, L., Bravo‐Rodriguez, K., Redel, A., Kostova, S., McShane, E., Opitz, R. J., Faelber, K., et al. (2016) · Nature Communications · doi:10.1038/ncomms13047 · Cited by 43
Encephalitis is mediated by ROP18 of Toxoplasma gondii , a severe pathogen in AIDS patients
An, R., Tang, Y., Chen, L., Cai, H., Lai, D., Liu, K., Wan, L., Gong, L., Yu, L., Luo, Q., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1801118115 · Cited by 43
The effect of statin therapy on endoplasmic reticulum stress
Mollazadeh, H., Atkin, S. L., Butler, A. E., Ruscica, M., Sirtori, C. R., & Sahebkar, A. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.10.006 · Cited by 42
Camalexin Induces Apoptosis via the ROS‐ER Stress‐Mitochondrial Apoptosis Pathway in AML Cells
Yang, Y., Wang, G., Wu, W., Yao, S., Han, X., He, D., He, J., Zheng, G., Zhao, Y., Cai, Z., et al. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/7426950 · Cited by 43
KLF6 Induces Apoptosis in Human Lens Epithelial Cells Through the ATF4-ATF3-CHOP Axis
Tian, F., Zhao, J., Bu, S., He, T., Yang, J., Zhang, X., Li, X., & Dong, L. (2020) · Drug Design Development and Therapy · doi:10.2147/dddt.s218467 · Cited by 45
Resistance to the Proteasome Inhibitors: Lessons from Multiple Myeloma and Mantle Cell Lymphoma
Gonzalez-Santamarta, M., Quinet, G., Reyes-Garau, D., Sola, B., Roué, G., & Rodríguez, M. S. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_6 · Cited by 46
The protective effect of natural compounds against rotenone‐induced neurotoxicity
Yarmohammadi, F., Hayes, A. W., Najafi, N., & Karimi, G. (2020) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22605 · Cited by 43
Krishnamoorthy, J., Rajesh, K., Mirzajani, F., Kesoglidou, P.-X., Papadakis, A. I., & Koromilas, A. E. (2014) · Cell Cycle · doi:10.4161/cc.27726 · Cited by 43
Metadata
- Authors
- Szegezdi, E., Logue, S. E., Gorman, A. M., & Samali, A.
- Affiliations
- National University of Ireland (IE)
- Venue
- The EMBO Reports
- Published
- 2006-09-01
- Volume
- 7
- Issue
- 9
- Pages
- 880-885
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1559676
- OpenAlex
- W2133644385
- Cited by
- 2,345
- References
- 45
- Citations by year
- 2026: 42 · 2025: 85 · 2024: 121 · 2023: 129 · 2022: 147 · 2021: 126 · 2020: 147 · 2019: 139 · 2018: 154 · 2017: 140 · 2016: 140 · 2015: 140 · 2014: 137 · 2013: 134 · 2012: 124
- FWCI
- 5.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Arrow@dit (Dublin Institute of Technology) (submittedVersion)
- ARAN (University of Galway Research Repository) (Ollscoil na Gaillimhe – University of Galway) (submittedVersion, cc-by-nc-nd)
- Funders
- Science Foundation Ireland
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- endoplasmic reticulum stress, apoptosis, unfolded protein response, ER stress-induced apoptosis, unfolded proteins, neurodegenerative diseases, cardiovascular disease, cell death mechanisms
- MeSH terms
- Animals, Endoplasmic Reticulum, Humans, Models, Biological, Signal Transduction, Apoptosis, Protein Folding, Oxidative Stress, Molecular Chaperones, Protein Transport, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review